Although the sulfate/anion transporter (sat-1; SLC26A1) was isolated from a rat liver cDNA library by expression cloning, localization of sat-1 within the liver and its contribution to the transport of sulfate and organo sulfates have remained unresolved. In situ hybridization and immunohistochemical studies were undertaken to demonstrate the localization of sat-1 in liver tissue. RT-PCR studies on isolated hepatocytes and liver endothelial and stellate cells in culture were performed to test for the presence of sat-1 in these cells. In sulfate uptake and efflux experiments, the substrate specificity of sat-1 was evaluated. Sat-1 mRNA was found in hepatocytes and endothelial cells. Sat-1 protein was localized in sinusoidal membranes and along the borders of hepatocytes. The canalicular region and bile capillaries were not stained. Sulfate uptake was only slightly affected by sulfamoyl diuretics or organo sulfates. Sulfate efflux from sat-1-expressing oocytes was enhanced in the presence of bicarbonate, indicating sulfate/bicarbonate exchange. Estrone sulfate was not transported by sat-1. Sat-1 may be responsible for the uptake of inorganic sulfate from the blood into hepatocytes to enable sulfation reactions. In hepatocytes and endothelial cells, sat-1 may also supply sulfate for proteoglycan synthesis.
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http://dx.doi.org/10.1152/ajpgi.00492.2005 | DOI Listing |
BMC Vet Res
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Aklilu Lemma Institute of Pathobiology (AAU-ALIPB), Addis Ababa University, Addis Ababa, Ethiopia.
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Institute of Ecological Restoration, College of Industrial Sciences, Kongju National University, Yesan-gun, Chungcheongnam-do, Republic of Korea.
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Institute of Cell Biology, University of Bern, Baltzerstrasse 4, 3006 Bern, Switzerland; Multidisciplinary Center for Infectious Diseases, University of Bern, Hallerstrasse 6, 3012 Bern, Switzerland; Institute for Infectious Diseases, University of Bern, Friedbuehlstrasse 25, 3001 Bern, Switzerland. Electronic address:
Functional gene and protein characterizations in parasitic protists are often limited by their genetic tractability. Despite the development of CRISPR-Cas9-derived or inspired approaches for a handful of protist parasites, the overall genetic tractability of these organisms remains limited. The intestinal parasite Giardia lamblia is one such species, with the added challenge of a paucity of reliable selection markers.
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